RUcore: Rutgers University Community Repository
Studies of polyadenylation regulation of U1A mRNA by an RNP complex containing U1A and U1 snRNP
Descriptive
TypeOfResource
Text
TitleInfo
(ID = T-1)
Title
Studies of polyadenylation regulation of U1A mRNA by an RNP complex containing U1A and U1 snRNP
Identifier
ETD_3119
Identifier
(type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000057530
Language
LanguageTerm
(authority = ISO639-2);
(type = code)
eng
Genre
(authority = marcgt)
theses
Subject
(ID = SBJ-1);
(authority = RUETD)
Topic
Biochemistry
Subject
(ID = SBJ-2);
(authority = ETD-LCSH)
Topic
Gene expression
Subject
(ID = SBJ-3);
(authority = ETD-LCSH)
Topic
Genetic regulation
Subject
(ID = SBJ-4);
(authority = ETD-LCSH)
Topic
RNA
Abstract
(type = abstract)
The 3’-end processing of nearly all eukaryotic pre-mRNAs comprises multiple steps which culminate in the addition of a poly(A) tail, which is essential for mRNA stability, translation, and export. Consequently, polyadenylation regulation is an important component of gene expression. One way to regulate polyadenylation is to inhibit the activity of a single poly(A) site, as exemplified by the U1A protein that negatively autoregulates itself by binding to a Polyadenylation Inhibitory Element (PIE) site within the 3’ UTR of its own pre-mRNA. U1 snRNP, which is primarily involved in splice site recognition, inhibits poly(A) site activity in papillomaviruses by binding to 5’ splice site-like sequences, which have recently been named “U1-sites”. Here, a recently identified U1-site in the human U1A 3'UTR is examined and shown to synergize with the adjacent PIE site to inhibit polyadenylation. However, unlike the sites found in papillomaviruses, the U1A U1-site has no inhibitory activity on its own and is dependent on a wild-type PIE. This lack of activity is due to the site being masked within a phylogenetically conserved stem structure (U1-STEM). The secondary RNA structure of this region was confirmed by RNase digestion analysis. Mutation of the U1-STEM, thereby opening up the U1-site, greatly increases U1-site mediated inhibition. The region between the U1-STEM and PIE (referred to as Region C) was also revealed to be required for synergy. Since biotin pulldown assays indicated that U1 snRNP binding to the U1-site was not affected by the presence of the U1-STEM, a model was proposed suggesting that U1 snRNP binds to the U1-STEM, but remains trapped in an inactive conformation until PIE is bound by two U1A molecules. However, further experiments showed that U1 snRNP binding did actually increase when the U1-STEM was mutated, but no corresponding change to the U1-STEM structure was detected. The discrepancies within these data suggest there is still much to be determined regarding the binding of U1 snRNP to the U1-Site. A more refined model is then presented which involves remodeling of Region C and part of the U1-STEM.
PhysicalDescription
Form
(authority = gmd)
electronic resource
Extent
ix, 133 p. : ill.
InternetMediaType
application/pdf
InternetMediaType
text/xml
Note
(type = degree)
Ph.D.
Note
(type = bibliography)
Includes bibliographical references
Note
(type = vita)
Includes vita
Note
(type = statement of responsibility)
by Rose Marie Caratozzolo
Name
(ID = NAME-1);
(type = personal)
NamePart
(type = family)
Caratozzolo
NamePart
(type = given)
Rose Marie
NamePart
(type = date)
1978-
Role
RoleTerm
(authority = RULIB)
author
DisplayForm
Rose Marie Caratozzolo
Name
(ID = NAME-2);
(type = personal)
NamePart
(type = family)
GUNDERSON
NamePart
(type = given)
SAMUEL I
Role
RoleTerm
(authority = RULIB)
chair
Affiliation
Advisory Committee
DisplayForm
SAMUEL I GUNDERSON
Name
(ID = NAME-3);
(type = personal)
NamePart
(type = family)
Brewer
NamePart
(type = given)
Gary
Role
RoleTerm
(authority = RULIB)
internal member
Affiliation
Advisory Committee
DisplayForm
Gary Brewer
Name
(ID = NAME-4);
(type = personal)
NamePart
(type = family)
Covey
NamePart
(type = given)
Lori
Role
RoleTerm
(authority = RULIB)
internal member
Affiliation
Advisory Committee
DisplayForm
Lori Covey
Name
(ID = NAME-5);
(type = personal)
NamePart
(type = family)
Tian
NamePart
(type = given)
Bin
Role
RoleTerm
(authority = RULIB)
outside member
Affiliation
Advisory Committee
DisplayForm
Bin Tian
Name
(ID = NAME-1);
(type = corporate)
NamePart
Rutgers University
Role
RoleTerm
(authority = RULIB)
degree grantor
Name
(ID = NAME-2);
(type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm
(authority = RULIB)
school
OriginInfo
DateCreated
(qualifier = exact)
2011
DateOther
(qualifier = exact);
(type = degree)
2011-01
Place
PlaceTerm
(type = code)
xx
RelatedItem
(type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier
(type = RULIB)
ETD
RelatedItem
(type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier
(type = local)
rucore19991600001
Location
PhysicalLocation
(authority = marcorg);
(displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier
(type = doi)
doi:10.7282/T3NS0TJ1
Genre
(authority = ExL-Esploro)
ETD doctoral
Back to the top
Rights
RightsDeclaration
(AUTHORITY = GS);
(ID = rulibRdec0006)
The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
RightsHolder
(ID = PRH-1);
(type = personal)
Name
FamilyName
Caratozzolo
GivenName
Rose Marie
Role
Copyright Holder
RightsEvent
(ID = RE-1);
(AUTHORITY = rulib)
Type
Permission or license
DateTime
2011-01-04 21:12:17
AssociatedEntity
(ID = AE-1);
(AUTHORITY = rulib)
Role
Copyright holder
Name
Rose Marie Caratozzolo
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject
(ID = AO-1);
(AUTHORITY = rulib)
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
Back to the top
Technical
ContentModel
ETD
MimeType
(TYPE = file)
application/pdf
MimeType
(TYPE = container)
application/x-tar
FileSize
(UNIT = bytes)
2088960
Checksum
(METHOD = SHA1)
ef87d77aa10c597cb3c8c6df54978bf7a7192fc6
Back to the top
Statistical Profile